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  Protein-free division of giant unilamellar vesicles controlled by enzymatic activity

Dreher, Y., Spatz, J. P., & Göpfrich, K. (2019). Protein-free division of giant unilamellar vesicles controlled by enzymatic activity. bioRxiv, e-pup: 881557, pp. 1-24. doi:10.1101/2019.12.30.881557.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0005-7011-9 Version Permalink: https://hdl.handle.net/21.11116/0000-0005-7012-8
Genre: Journal Article

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 Creators:
Dreher, Yannik1, Author           
Spatz, Joachim P.2, 3, Author           
Göpfrich, Kerstin2, Author           
Affiliations:
1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
3Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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 Abstract: Cell division is one of the hallmarks of life. Success in the bottom-up assembly of synthetic cells will, no doubt, depend on strategies for the controlled autonomous division of protocellular compartments. Here, we describe the protein-free division of giant unilamellar lipid vesicles (GUVs) based on the combination of two physical principles – phase separation and osmosis. We visualize the division process with confocal fluorescence microscopy and derive a conceptual model based on the vesicle geometry. The model successfully predicts the shape transformations over time as well as the time point of the final pinching of the daughter vesicles. Remarkably, we show that two fundamentally distinct yet highly abundant processes – water evaporation and metabolic activity – can both regulate the autonomous division of GUVs. Our work may hint towards mechanisms that governed the division of protocells and adds to the strategic toolbox of bottom-up synthetic biology with its vision of bringing matter to life.

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Language(s): eng - English
 Dates: 2019-12-30
 Publication Status: Issued
 Pages: 24
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1101/2019.12.30.881557
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Title: bioRxiv
Source Genre: Collected Edition
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Publ. Info: NY : Cold Spring Harbor Laboratory
Pages: - Volume / Issue: e-pup Sequence Number: 881557 Start / End Page: 1 - 24 Identifier: -